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Conserved domains on  [gi|24585626|ref|NP_610102|]
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lethal (2) k14505, isoform A [Drosophila melanogaster]

Protein Classification

ATP12 family chaperone protein( domain architecture ID 10540317)

ATP12 family chaperone protein similar to Saccharomyces cerevisiae mitochondrial protein ATP12, which is essential for the assembly of the mitochondrial F1-F0 complex

Gene Ontology:  GO:0043461
SCOP:  4002624

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATP12 pfam07542
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
39-157 4.08e-48

ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.


:

Pssm-ID: 462201  Cd Length: 121  Bit Score: 156.10  E-value: 4.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626    39 RFYKKTSVLSGDSGYEVVLDHRKLKTPKGTPFIVRSEPLAIAVATEFDAQKENIERSRMHLSALCFTAID--NPNHLSKL 116
Cdd:pfam07542   1 RFWKEVSVEEVDGGFEVLLDGRPLRTPSGNPLAVPSEKLAEAIAAEWDAQGETIKPHSMPLTSLASRAIDlrVPDAGDRE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24585626   117 DMVNYLLNFIATDTVLFQYDDEKDLQDLQVNEWDPVIAWFN 157
Cdd:pfam07542  81 AIVDDLLRYLDTDTLLYRAEEPEALRARQAEAWDPLLDWAE 121
 
Name Accession Description Interval E-value
ATP12 pfam07542
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
39-157 4.08e-48

ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.


Pssm-ID: 462201  Cd Length: 121  Bit Score: 156.10  E-value: 4.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626    39 RFYKKTSVLSGDSGYEVVLDHRKLKTPKGTPFIVRSEPLAIAVATEFDAQKENIERSRMHLSALCFTAID--NPNHLSKL 116
Cdd:pfam07542   1 RFWKEVSVEEVDGGFEVLLDGRPLRTPSGNPLAVPSEKLAEAIAAEWDAQGETIKPHSMPLTSLASRAIDlrVPDAGDRE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24585626   117 DMVNYLLNFIATDTVLFQYDDEKDLQDLQVNEWDPVIAWFN 157
Cdd:pfam07542  81 AIVDDLLRYLDTDTLLYRAEEPEALRARQAEAWDPLLDWAE 121
Atp12 COG5387
Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, ...
37-266 4.85e-44

Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444150  Cd Length: 235  Bit Score: 149.18  E-value: 4.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626  37 PKRFYKKTSVLSGDSGYEVVLDHRKLKTPKGTPFIVRSEPLAIAVATEFDAQKENIERSRMHLSALCFTAIDN--PNHLS 114
Cdd:COG5387   5 PKRFYKEATVAEAEGGFAVLLDGRPVRTPAKAPLVVPTRALAEAIAAEWAAQGEEIDPATMPLTRLANTAIDRvaPQRAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626 115 KLDMvnyLLNFIATDTVLFQYDDEKDLQDLQVNEWDPVIAWFNQRYDTNLQKTMNITP-PQvSEQDKMNVAKHFQSYSLE 193
Cdd:COG5387  85 VADE---LAAYAGSDLLCYRADSPEELVARQAAAWDPLLDWAAERLGARLVLTEGVMHvPQ-PPEALAALRAALEALDPF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626 194 TLHGFIFAVDTLKSIVLACAVIEQMLTVEKAVALARLEEEYQLKFWGRVEwahdlsqqELQARLA-------AAVLFVHL 266
Cdd:COG5387 161 RLAALHDLTTLTGSLVLALALAEGRLDAEEAWAAAHLDEDWQIEQWGEDE--------EAAARRAarraeflAAARFLDL 232
 
Name Accession Description Interval E-value
ATP12 pfam07542
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
39-157 4.08e-48

ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.


Pssm-ID: 462201  Cd Length: 121  Bit Score: 156.10  E-value: 4.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626    39 RFYKKTSVLSGDSGYEVVLDHRKLKTPKGTPFIVRSEPLAIAVATEFDAQKENIERSRMHLSALCFTAID--NPNHLSKL 116
Cdd:pfam07542   1 RFWKEVSVEEVDGGFEVLLDGRPLRTPSGNPLAVPSEKLAEAIAAEWDAQGETIKPHSMPLTSLASRAIDlrVPDAGDRE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24585626   117 DMVNYLLNFIATDTVLFQYDDEKDLQDLQVNEWDPVIAWFN 157
Cdd:pfam07542  81 AIVDDLLRYLDTDTLLYRAEEPEALRARQAEAWDPLLDWAE 121
Atp12 COG5387
Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, ...
37-266 4.85e-44

Mitochondrial FoF1-type ATP synthase assembly chaperone ATP12 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444150  Cd Length: 235  Bit Score: 149.18  E-value: 4.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626  37 PKRFYKKTSVLSGDSGYEVVLDHRKLKTPKGTPFIVRSEPLAIAVATEFDAQKENIERSRMHLSALCFTAIDN--PNHLS 114
Cdd:COG5387   5 PKRFYKEATVAEAEGGFAVLLDGRPVRTPAKAPLVVPTRALAEAIAAEWAAQGEEIDPATMPLTRLANTAIDRvaPQRAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626 115 KLDMvnyLLNFIATDTVLFQYDDEKDLQDLQVNEWDPVIAWFNQRYDTNLQKTMNITP-PQvSEQDKMNVAKHFQSYSLE 193
Cdd:COG5387  85 VADE---LAAYAGSDLLCYRADSPEELVARQAAAWDPLLDWAAERLGARLVLTEGVMHvPQ-PPEALAALRAALEALDPF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585626 194 TLHGFIFAVDTLKSIVLACAVIEQMLTVEKAVALARLEEEYQLKFWGRVEwahdlsqqELQARLA-------AAVLFVHL 266
Cdd:COG5387 161 RLAALHDLTTLTGSLVLALALAEGRLDAEEAWAAAHLDEDWQIEQWGEDE--------EAAARRAarraeflAAARFLDL 232
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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